ID   TOP3_STAEQ              Reviewed;         711 AA.
AC   Q5HLZ4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=DNA topoisomerase 3 {ECO:0000255|HAMAP-Rule:MF_00953};
DE            EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00953};
DE   AltName: Full=DNA topoisomerase III {ECO:0000255|HAMAP-Rule:MF_00953};
GN   Name=topB {ECO:0000255|HAMAP-Rule:MF_00953};
GN   OrderedLocusNames=SERP1836;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC       is introduced during the DNA replication and transcription, by
CC       transiently cleaving and rejoining one strand of the DNA duplex.
CC       Introduces a single-strand break via transesterification at a target
CC       site in duplex DNA. The scissile phosphodiester is attacked by the
CC       catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC       (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC       DNA strand. The free DNA strand then undergoes passage around the
CC       unbroken strand, thus removing DNA supercoils. Finally, in the
CC       religation step, the DNA 3'-OH attacks the covalent intermediate to
CC       expel the active-site tyrosine and restore the DNA phosphodiester
CC       backbone. {ECO:0000255|HAMAP-Rule:MF_00953}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00953};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00953};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00953, ECO:0000255|PROSITE-
CC       ProRule:PRU01383}.
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DR   EMBL; CP000029; AAW55174.1; -; Genomic_DNA.
DR   RefSeq; WP_002456984.1; NC_002976.3.
DR   AlphaFoldDB; Q5HLZ4; -.
DR   SMR; Q5HLZ4; -.
DR   STRING; 176279.SERP1836; -.
DR   KEGG; ser:SERP1836; -.
DR   eggNOG; COG0550; Bacteria.
DR   eggNOG; COG0551; Bacteria.
DR   HOGENOM; CLU_002929_5_2_9; -.
DR   Proteomes; UP000000531; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   HAMAP; MF_00953; Topoisom_3_prok; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR023406; Topo_IA_AS.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR005738; TopoIII.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   NCBIfam; TIGR01056; topB; 1.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   PROSITE; PS00396; TOPO_IA_1; 1.
DR   PROSITE; PS52039; TOPO_IA_2; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Isomerase; Magnesium; Metal-binding; Reference proteome;
KW   Topoisomerase.
FT   CHAIN           1..711
FT                   /note="DNA topoisomerase 3"
FT                   /id="PRO_0000286376"
FT   DOMAIN          2..135
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   DOMAIN          152..580
FT                   /note="Topo IA-type catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   REGION          186..191
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   ACT_SITE        305
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01383"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   BINDING         104
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   SITE            60
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   SITE            167
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   SITE            175
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
FT   SITE            307
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00953"
SQ   SEQUENCE   711 AA;  82393 MW;  13AB643F53065FB9 CRC64;
     MKSLILAEKP SVGRDIANAL NLQQKSNGYI EGKQYIVTWA LGHLVTNATP EQYNPSYKEW
     NLEDLPIIPK KMKTVVISKT NRQFKIVKSL ILDKNVKEII IATDAGREGE LVARLILDKV
     GNKKPIKRLW ISSVTKKAIQ EGFKQLKNGN AYQNLYEAAL ARSEADWIVG INATRALTTK
     YDAQLSLGRV QTPTIQIVKS RQDEINYFKP EKYYTLSINV DGYDLNLKQQ KRYKDKKELE
     LIEHKIKHQE GKILEVKGKN KKSYAQPLFN LTDLQQEAYK HYKMGPKETL NTLQHLYERH
     KLVTYPRTDS NYLTDDMVDT IQERLRAILA TDYKSHVRDL ISESFSSKMH IFNNQKVSDH
     HAIIPTEVRP SIEQLSQREF KIYMLIAERF LENLMNPYLY EVLTIHAQLK DYNFVLKEII
     PKQLGYKALK DQTSSHTLTH SFKEGQLFKV HRIEIHEHET KAPEYFNEGS LLKAMENPQN
     HIDLNDKKYA KTLKHSGGIG TVATRADIIE KLFNMNALES RDGKIKVTSK GKQILELSPS
     ELTSPILTAQ WEEKLMLIEK GKYNSQKFIQ EMKNFTFKVV NKIKSSEQKY KHDNLTTTEC
     PTCGKFMIKV KTKNGQMLVC QDPKCKTKKN IQRKTNARCP YCKKKMTLFG KGKEAVYRCV
     CGHTETQSQM DKRMRDKTNG KVSRKEMKKY INKKEEIDNN PFKDALKNLK L
//